Structural highlights
Function
FIMA1_ECOLI Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Publication Abstract from PubMed
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-A resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable "spring-like" properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.
The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.,Hospenthal MK, Zyla D, Costa TRD, Redzej A, Giese C, Lillington J, Glockshuber R, Waksman G Structure. 2017 Nov 7. pii: S0969-2126(17)30332-5. doi:, 10.1016/j.str.2017.10.004. PMID:29129382[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hospenthal MK, Zyla D, Costa TRD, Redzej A, Giese C, Lillington J, Glockshuber R, Waksman G. The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod. Structure. 2017 Nov 7. pii: S0969-2126(17)30332-5. doi:, 10.1016/j.str.2017.10.004. PMID:29129382 doi:http://dx.doi.org/10.1016/j.str.2017.10.004
